Recombinant Human SUMO1 AMC Protein, CF

Product Discontinued

Recombinant Human SUMO1 AMC Protein, CF Summary

• Details of Functionality: Recombinant Human SUMO1 AMC is a fluorogenic substrate for some SUMO-specific isopeptidases. Release of AMC fluorescence can be monitored with an excitation wavelength of 345 nM and an emission wavelength of 445 nM. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human SUMO1 AMC concentration of 0.1-1 μM.
• Source: E. coli-derived human SUMO1 protein
• Accession #: P63165
• Protein/Peptide Type: Recombinant Proteins
• Gene: SUMO1
• Purity: >95%, by HPLC.

Applications/Dilutions

• Dilutions:
  • Enzyme Activity
• Theoretical MW: 11 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
• Buffer:

  1.13 mg/ml (100 µM) in 50 mM HEPES pH 7.5, 100 mM NaCl

• Purity: >95%, by HPLC.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human SUMO1 AMC Protein, CF

• DAP1
• GAP modifying protein 1
• GAP-modifying protein 1
• GMP1SMT3CSMT3H3OFC10UBL1PIC1
• PIC1
• SENP2
• Sentrin
• small ubiquitin-related modifier 1
• SMT3 homolog 3
• SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae)
• SMT3 suppressor of mif two 3 homolog 1 (yeast)
• SMT3
• SMT3C
• SMT3H3
• SUMO1
• SUMO-1
• Ubiquitin-homology domain protein PIC1
• ubiquitin-like 1 (sentrin)
• Ubiquitin-like protein SMT3C
• Ubiquitin-like protein UBL1
• UBL1

Background

Human Small Ubiquitin-like Modifier 1 (SUMO1), also known as Sentrin, UBL1, and SMT3C, is synthesized as a 101 amino acid (aa) propeptide with a predicted molecular weight of 11.5 kDa. Human SUMO1 is the most unique of the four identified SUMO proteins and shares only 44%, 47%, and 41% aa sequence identity with SUMO2, SUMO3, and SUMO4, respectively. In contrast, human SUMO1 shares 100% aa sequence identity with the mouse ortholog. SUMOs are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation (1-3). All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following cleavage of a four aa C-terminal prosegment, the C-terminal glycine residue of SUMO1 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO1 is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme (4,5). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (6). SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO1 is transferred directly from UBE2I/Ubc9 to specific substrates. In Alzheimer's disease models SUMO1 has been shown to influence the generation of Amyloid-beta peptide by promoting the accumulation of BACE-1 (7). Covalent modification of Phosphatase and Tensin Homolog Deleted on Chromosome (PTEN) by SUMO1 is thought to regulate tumorigenesis by retaining PTEN at the plasma membrane, an effect that suppresses PI 3-Kinase/Akt-dependent tumor growth (8).

This fluorogenic substrate for SUMO1 hydrolases is based on the carboxy-terminus derivatization of SUMO1 with 7-amido-4-methylcoumarin (AMC). SUMO1 AMC is useful for studying SUMO1 hydrolases when detection sensitivity or continuous monitoring of activity is essential.

1. Desterro, J.M. et al. (1997) FEBS. Lett. 417:297.
2. Bettermann, K. et al. (2012) Cancer Lett. 316:113.
3. Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
4. Okuma, T. et al. (1999) Biochem. Biophys. Res.  Commun. 254:693.
5. Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
6. Johnson, E.S. et al. (1997) EMBO J. 16:5509.
7. Yun, S.M. et al. (2013) Neurobiol Aging. 34:650.
8. Huang, J. et al. (2012) Nat. Commun. 3:911.

Publications for SUMO1 (UL-551)(6)

Publications using UL-551

• M Brand, EB Bommeli, M Rütimann, U Lindenmann, R Riedl Discovery of a Dual SENP1 and SENP2 Inhibitor International Journal of Molecular Sciences, 2022-10-11;23(20):. 2022-10-11 [PMID: 36292935] (Bioassay)
• P Paudel, Q Zhang, C Leung, HC Greenberg, Y Guo, YH Chern, A Dong, Y Li, M Vedadi, Z Zhuang, Y Tong Crystal structure and activity-based labeling reveal the mechanisms for linkage-specific substrate recognition by deubiquitinase USP9X Proc. Natl. Acad. Sci. U.S.A., 2019-03-26;0(0):. 2019-03-26 [PMID: 30914461] (Bioassay)
• F Rodríguez-, RB Lemma, I Cuervo, M Bengtsen, LM Moen, M Ledsaak, R Eskeland, OS Gabrielsen The SUMO protease SENP1 and the chromatin remodeller CHD3 interact and jointly affect chromatin accessibility and gene expression J. Biol. Chem., 2018-08-06;0(0):. 2018-08-06 [PMID: 30082317]
• P Lapaquette, S Fritah, N Lhocine, A Andrieux, G Nigro, J Mounier, P Sansonetti, A Dejean Shigella entry unveils a calcium/calpain-dependent mechanism for inhibiting sumoylation Elife, 2017-12-12;6(0):. 2017-12-12 [PMID: 29231810] (Bioassay)
• Malene L Urbanus Diverse mechanisms of metaeffector activity in an intracellular bacterial pathogen, Legionella pneumophila Mol. Syst. Biol, 2016-12-16;12(12):893. 2016-12-16 [PMID: 27986836] (Bioassay)
• Liang , Qin, Dexheimer , Thomas S, Zhang , Ping, Rosenthal , Andrew S, Villamil , Mark A, You , Changjun, Zhang , Qiuting, Chen , Junjun, Ott , Christin, Sun , Hongmao, Luci , Diane K, Yuan , Bifeng, Simeonov , Anton, Jadhav , Ajit, Xiao , Hui, Wang , Yinsheng, Maloney , David J, Zhuang , Zhihao A selective USP1-UAF1 inhibitor links deubiquitination to DNA damage responses. Nat Chem Biol, 2014-02-16;10(4):298-304. 2014-02-16 [PMID: 24531842] (Bioassay)

Bioinformatics

• Gene Symbol: SUMO1
• Uniprot:
  • P63165()